Determining the three-dimensional structure of proteins contributes to our understanding of how living organisms function and to the development of new therapies. While artificial intelligence has recently revolutionised this field, structural data remains essential for validating models and gaining access to many proteins that are still unknown. However, obtaining reliable data relies largely on X-ray crystallography. This powerful technique, which can be combined with high-throughput screening methods, requires several conditions to be met: the production of high-quality protein crystals, their rapid and selective identification, and the resolution of structures from X-ray diffraction data.
A new molecular tool called Imaging-Crystallophore could significantly simplify and speed up the work of structural biologists by providing a combined solution to the problem of protein crystallisation and the detection of the resulting crystals.
This tool is described in an article published in Angewandte Chemie International Edition.
To know more (in French) :
Actualités - CNRS Chimie
Collaborations :
Laboratoire de chimie (CNRS/ENS Lyon/Université Lyon 1)
Institut de Biologie Structurale (CNRS/CEA/UGA)
Université Côte d’Azur
EMBL
Société Polyvalan